Molecular dynamics (CHARMM) techniques are proposed for the study of the incorporation of amphiphilic peptides in membrane, the orientation of these peptides with respect to the membrane/water interface, and the conformation of the peptides in these environments. Two membrane mimics will be used for this study. One is a biphasic model of water/CC14, the other is micelles formed by sodium dodecylsulfate (SDS). Two series of small neuropeptides, which contain primary amphiphilic moments, will be used for this work. The goals fo this work are to compare the results on the incorporation and orientation of the peptides (with respect to the membrane/water interface) in these two membrane mimics and to combine the MD simulation in these media with NMR distance constraints obtained from NMR of these peptides in SDS micelles to determine the conformation of the peptides in the same membrane mimic environment. Molecular dynamics (CHARMM) techniques are proposed for the study of the incorporation of amphiphilic peptides in membrane, the orientation of these peptides with respect to the membrane/water interface, and the conformation of the peptides in these environments. Two membrane mimics will be used for this study. One is a biphasic model of water/CC14, the other is micelles formed by sodium dodecylsulfate (SDS). Two series of small neuropeptides, which contain primary amphiphilic moments, will be used for this work. The goals for this work are to compare the results on the incorporation and orientation of the peptides (with respect to the membrane/water interface) in these two membrane mimics and to combine the MD simulation in these media with NMR distance constraints obtained from NMR of these peptides in SDS micelles to determine the conformation of the peptides in the same membrane mimic environment.